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Volumn 417, Issue 1, 2009, Pages 1-13

How mitochondria produce reactive oxygen species

Author keywords

Complex I; Hydrogen peroxide; Mitochondrion; Reactive oxygen species (ROS); Respiratory chain; Superoxide

Indexed keywords

COMPLEX I; CONCENTRATION OF; CYTOSOL; ELECTRON DONORS; IN-VIVO; MATRIX; MITOCHONDRIAL MATRIX; MODES OF OPERATION; OXIDATIVE DAMAGE; PRODUCTION RATES; PROTON-MOTIVE FORCES; REACTIVE OXYGEN SPECIES; REACTIVE OXYGEN SPECIES (ROS); REDOX SIGNALLING; RESPIRATORY CHAIN; SECOND-ORDER RATE CONSTANTS; SUPEROXIDE;

EID: 58249093939     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20081386     Document Type: Review
Times cited : (6147)

References (132)
  • 2
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens, J. F. (2003) Mitochondrial formation of reactive oxygen species. J. Physiol. 552, 335-344
    • (2003) J. Physiol , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 3
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban, R. S., Nemoto, S. and Finkel, T. (2005) Mitochondria, oxidants, and aging. Cell 120, 483-495
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 4
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance, B., Sies, H. and Boveris, A. (1979) Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59, 527-605
    • (1979) Physiol. Rev , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 5
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • Cadenas, E. and Davies, K. J. (2000) Mitochondrial free radical generation, oxidative stress, and aging. Free Radical Biol. Med. 29, 222-230
    • (2000) Free Radical Biol. Med , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 6
    • 0034306267 scopus 로고    scopus 로고
    • Mitochondria, oxygen free radicals, disease and ageing
    • Raha, S. and Robinson, B. H. (2000) Mitochondria, oxygen free radicals, disease and ageing. Trends Biochem. 25, 502-508
    • (2000) Trends Biochem , vol.25 , pp. 502-508
    • Raha, S.1    Robinson, B.H.2
  • 7
    • 33751072935 scopus 로고    scopus 로고
    • Bioenergetics and the formation of mitochondrial reactive oxygen species
    • Adam-Vizi, V. and Chinopoulos, C. (2006) Bioenergetics and the formation of mitochondrial reactive oxygen species. Trends Pharmacol. Sci. 27, 639-645
    • (2006) Trends Pharmacol. Sci , vol.27 , pp. 639-645
    • Adam-Vizi, V.1    Chinopoulos, C.2
  • 8
    • 0034442070 scopus 로고    scopus 로고
    • The nature and mechanism of superoxide production by the electron transport chain
    • Muller, F. (2000) The nature and mechanism of superoxide production by the electron transport chain. J. Am. Aging Assoc. 23, 227-253
    • (2000) J. Am. Aging Assoc , vol.23 , pp. 227-253
    • Muller, F.1
  • 9
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge, W. (2002) Free radicals in the physiological control of cell function. Physiol. Rev. 82, 47-95
    • (2002) Physiol. Rev , vol.82 , pp. 47-95
    • Droge, W.1
  • 10
    • 0014010888 scopus 로고
    • Antimycin-insensitive oxidation of succinate and reduced nicotinamide-adenine dinucleotide in electron-transport particles. I. pH dependency and hydrogen peroxide formation
    • Jensen, P. K. (1966) Antimycin-insensitive oxidation of succinate and reduced nicotinamide-adenine dinucleotide in electron-transport particles. I. pH dependency and hydrogen peroxide formation. Biochim. Biophys. Acta 122, 157-166
    • (1966) Biochim. Biophys. Acta , vol.122 , pp. 157-166
    • Jensen, P.K.1
  • 12
    • 0015882341 scopus 로고
    • The mitochondrial generation of hydrogen peroxide: General properties and effect of hyperbaric oxygen
    • Boveris, A. and Chance, B. (1973) The mitochondrial generation of hydrogen peroxide: general properties and effect of hyperbaric oxygen. Biochem. J. 134, 707-716
    • (1973) Biochem. J , vol.134 , pp. 707-716
    • Boveris, A.1    Chance, B.2
  • 13
    • 0016148483 scopus 로고
    • Superoxide radicals as precursors of mitochondrial hydrogen peroxide
    • Loschen, G., Azzi, A., Richter, C. and Flohe, L. (1974) Superoxide radicals as precursors of mitochondrial hydrogen peroxide. FEBS Lett. 42, 68-72
    • (1974) FEBS Lett , vol.42 , pp. 68-72
    • Loschen, G.1    Azzi, A.2    Richter, C.3    Flohe, L.4
  • 14
    • 0016246294 scopus 로고
    • Role of superoxide radical in mitochondrial dehydrogenase reactions
    • Forman, H. J. and Kennedy, J. A. (1974) Role of superoxide radical in mitochondrial dehydrogenase reactions. Biochem. Biophys. Res. Commun. 60, 1044-1050
    • (1974) Biochem. Biophys. Res. Commun , vol.60 , pp. 1044-1050
    • Forman, H.J.1    Kennedy, J.A.2
  • 15
    • 0015848173 scopus 로고
    • Superoxide dismutase: Organelle specificity
    • Weisiger, R. A. and Fridovich, I. (1973) Superoxide dismutase: organelle specificity. J. Biol. Chem. 248, 3582-3592
    • (1973) J. Biol. Chem , vol.248 , pp. 3582-3592
    • Weisiger, R.A.1    Fridovich, I.2
  • 18
    • 0035160270 scopus 로고    scopus 로고
    • Tissue oxygen tension and brain sensitivity to hypoxia
    • Erecinska, M. and Silver, I. A. (2001) Tissue oxygen tension and brain sensitivity to hypoxia. Respir. Physiol. 128, 263-276
    • (2001) Respir. Physiol , vol.128 , pp. 263-276
    • Erecinska, M.1    Silver, I.A.2
  • 19
    • 0029765443 scopus 로고    scopus 로고
    • Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
    • Skulachev, V. P. (1996) Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants. Q. Rev. Biophys. 29, 169-202
    • (1996) Q. Rev. Biophys , vol.29 , pp. 169-202
    • Skulachev, V.P.1
  • 20
    • 0016732253 scopus 로고
    • Polarographic assay and intracellular distribution of superoxide dismutase in rat liver
    • Tyler, D. D. (1975) Polarographic assay and intracellular distribution of superoxide dismutase in rat liver. Biochem. J. 147, 493-504
    • (1975) Biochem. J , vol.147 , pp. 493-504
    • Tyler, D.D.1
  • 21
    • 0018129988 scopus 로고
    • Superoxide dismutase as an inhibitor of reactions of semiquinone radicals
    • Winterbourn, C. C., French, J. K. and Claridge, R. F. (1978) Superoxide dismutase as an inhibitor of reactions of semiquinone radicals. FEBS Lett. 94, 269-272
    • (1978) FEBS Lett , vol.94 , pp. 269-272
    • Winterbourn, C.C.1    French, J.K.2    Claridge, R.F.3
  • 22
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/ glutathione couple
    • Schafer, F. Q. and Buettner, G. R. (2001) Redox environment of the cell as viewed through the redox state of the glutathione disulfide/ glutathione couple. Free Radical Biol. Med. 30, 1191-1212
    • (2001) Free Radical Biol. Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 23
    • 0033369476 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical generation and leak: Sites of production in states 4 and 3, organ specificity, and relation to aging and longevity
    • Barja, G. (1999) Mitochondrial oxygen radical generation and leak: sites of production in states 4 and 3, organ specificity, and relation to aging and longevity. J. Bioenerg. Biomembr. 31, 347-366
    • (1999) J. Bioenerg. Biomembr , vol.31 , pp. 347-366
    • Barja, G.1
  • 24
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • St-Pierre, J., Buckingham, J. A., Roebuck, S. J. and Brand, M. D. (2002) Topology of superoxide production from different sites in the mitochondrial electron transport chain. J. Biol. Chem. 277, 44784-44790
    • (2002) J. Biol. Chem , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 26
    • 0020397137 scopus 로고
    • The effect of hyperoxia on superoxide production by lung submitochondrial particles
    • Turrens, J. F., Freeman, B. A., Levitt, J. G. and Crapo, J. D. (1982) The effect of hyperoxia on superoxide production by lung submitochondrial particles. Arch. Biochem. Biophys. 217, 401-410
    • (1982) Arch. Biochem. Biophys , vol.217 , pp. 401-410
    • Turrens, J.F.1    Freeman, B.A.2    Levitt, J.G.3    Crapo, J.D.4
  • 27
    • 1042301416 scopus 로고    scopus 로고
    • Characterization of superoxide-producing sites in isolated brain mitochondria
    • Kudin, A. P., Bimpong-Buta, N. Y., Vielhaber, S., Elger, C. E. and Kunz, W. S. (2004) Characterization of superoxide-producing sites in isolated brain mitochondria. J. Biol. Chem. 279, 4127-4135
    • (2004) J. Biol. Chem , vol.279 , pp. 4127-4135
    • Kudin, A.P.1    Bimpong-Buta, N.Y.2    Vielhaber, S.3    Elger, C.E.4    Kunz, W.S.5
  • 28
    • 33646716659 scopus 로고    scopus 로고
    • The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria
    • Kussmaul, L. and Hirst, J. (2006) The mechanism of superoxide production by NADH:ubiquinone oxidoreductase (complex I) from bovine heart mitochondria. Proc. Natl. Acad. Sci. U.S.A. 103, 7607-7612
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 7607-7612
    • Kussmaul, L.1    Hirst, J.2
  • 29
    • 33846225260 scopus 로고    scopus 로고
    • Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: Implications for hypoxic cell signaling
    • Hoffman, D. L., Salter, J. D. and Brookes, P. S. (2007) Response of mitochondrial reactive oxygen species generation to steady-state oxygen tension: implications for hypoxic cell signaling. Am. J. Physiol. Heart Circ. Physiol. 292, H101-H108
    • (2007) Am. J. Physiol. Heart Circ. Physiol , vol.292
    • Hoffman, D.L.1    Salter, J.D.2    Brookes, P.S.3
  • 31
    • 0035912784 scopus 로고    scopus 로고
    • Nitric oxide partitioning into mitochondrial membranes and the control of respiration at cytochrome c oxidase
    • Shiva, S., Brookes, P. S., Patel, R. P., Anderson, P. G. and Darley-Usmar, V. M. (2001) Nitric oxide partitioning into mitochondrial membranes and the control of respiration at cytochrome c oxidase. Proc. Natl. Acad. Sci. U.S.A. 98, 7212-7217
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 7212-7217
    • Shiva, S.1    Brookes, P.S.2    Patel, R.P.3    Anderson, P.G.4    Darley-Usmar, V.M.5
  • 32
    • 0028134892 scopus 로고
    • Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase
    • Brown, G. C. and Cooper, C. E. (1994) Nanomolar concentrations of nitric oxide reversibly inhibit synaptosomal respiration by competing with oxygen at cytochrome oxidase. FEBS Lett. 356, 295-298
    • (1994) FEBS Lett , vol.356 , pp. 295-298
    • Brown, G.C.1    Cooper, C.E.2
  • 33
    • 0029161636 scopus 로고
    • Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase
    • Brown, G. C. (1995) Nitric oxide regulates mitochondrial respiration and cell functions by inhibiting cytochrome oxidase. FEBS Lett. 369, 136-139
    • (1995) FEBS Lett , vol.369 , pp. 136-139
    • Brown, G.C.1
  • 34
    • 28044464985 scopus 로고
    • Reversible inhibition of cytochrome c oxidase, the terminal enzyme of mitochondrial respiratory chain, by nitric oxide
    • Cleeter, M. J. W., Cooper, J. M., Darley-Usmar, V. M., Moncada, S. and Schapira, A. H. V. (1994) Reversible inhibition of cytochrome c oxidase, the terminal enzyme of mitochondrial respiratory chain, by nitric oxide. FEBS Lett. 345, 50-54
    • (1994) FEBS Lett , vol.345 , pp. 50-54
    • Cleeter, M.J.W.1    Cooper, J.M.2    Darley-Usmar, V.M.3    Moncada, S.4    Schapira, A.H.V.5
  • 35
    • 0032947296 scopus 로고    scopus 로고
    • Nitric oxide and mitochondrial respiration
    • Brown, G. C. (1999) Nitric oxide and mitochondrial respiration. Biochim. Biophys. Acta 1411, 351-369
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 351-369
    • Brown, G.C.1
  • 36
    • 0346027211 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor-1α by nitric oxide through mitochondria-dependent and -independent pathways
    • Mateo, J., García-Lecea, M., Cadenas, S., Hernández, C. and Moncada, S. (2003) Regulation of hypoxia-inducible factor-1α by nitric oxide through mitochondria-dependent and -independent pathways. Biochem J. 376, 537-544
    • (2003) Biochem J , vol.376 , pp. 537-544
    • Mateo, J.1    García-Lecea, M.2    Cadenas, S.3    Hernández, C.4    Moncada, S.5
  • 37
    • 0348134741 scopus 로고    scopus 로고
    • Redistribution of intracellular oxygen in hypoxia by nitric oxide: Effect on HIF1α
    • Hagen, T., Taylor, C. T., Lam, F. and Moncada, S. (2003) Redistribution of intracellular oxygen in hypoxia by nitric oxide: effect on HIF1α. Science 302, 1975-1978
    • (2003) Science , vol.302 , pp. 1975-1978
    • Hagen, T.1    Taylor, C.T.2    Lam, F.3    Moncada, S.4
  • 38
    • 0036513249 scopus 로고    scopus 로고
    • Does nitric oxide modulate mitochondrial energy generation and apoptosis?
    • Moncada, S. and Erusalimsky, J. D. (2002) Does nitric oxide modulate mitochondrial energy generation and apoptosis? Nat. Rev. Mol. Cell Biol. 3, 214-220
    • (2002) Nat. Rev. Mol. Cell Biol , vol.3 , pp. 214-220
    • Moncada, S.1    Erusalimsky, J.D.2
  • 39
    • 34447638717 scopus 로고    scopus 로고
    • How do enzymes activate oxygen without inactivating themselves?
    • Klinman, J. P. (2007) How do enzymes activate oxygen without inactivating themselves? Acc. Chem. Res. 40, 325-333
    • (2007) Acc. Chem. Res , vol.40 , pp. 325-333
    • Klinman, J.P.1
  • 40
    • 0022004980 scopus 로고
    • Electron transfers in chemistry and biology
    • Marcus, R. A. and Sutin, N. (1985) Electron transfers in chemistry and biology. Biochim. Biophys. Acta 811, 265-322
    • (1985) Biochim. Biophys. Acta , vol.811 , pp. 265-322
    • Marcus, R.A.1    Sutin, N.2
  • 42
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavoproteins
    • Massey, V. (1994) Activation of molecular oxygen by flavins and flavoproteins. J. Biol. Chem. 269, 22459-22462
    • (1994) J. Biol. Chem , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 43
    • 0029086244 scopus 로고
    • A metabolic enzyme that rapidly produces superoxide, fumarate reductase of Escherichia coli
    • Imlay, J. A. (1995) A metabolic enzyme that rapidly produces superoxide, fumarate reductase of Escherichia coli. J. Biol. Chem. 270, 19767-19777
    • (1995) J. Biol. Chem , vol.270 , pp. 19767-19777
    • Imlay, J.A.1
  • 44
    • 38349105900 scopus 로고    scopus 로고
    • Complex I is the major site of mitochondrial superoxide production by paraquat
    • Cochemé, H. M. and Murphy, M. P. (2008) Complex I is the major site of mitochondrial superoxide production by paraquat. J. Biol. Chem. 283, 1786-1798
    • (2008) J. Biol. Chem , vol.283 , pp. 1786-1798
    • Cochemé, H.M.1    Murphy, M.P.2
  • 47
    • 17644394600 scopus 로고    scopus 로고
    • Detection and characterization of the product of hydroethidine and intracellular superoxide by HPLC and limitations of fluorescence
    • Zhao, H., Joseph, J., Fales, H. M., Sokoloski, E. A., Levine, R. L., Vasquez-Vivar, J. and Kalyanaraman, B. (2005) Detection and characterization of the product of hydroethidine and intracellular superoxide by HPLC and limitations of fluorescence. Proc. Natl. Acad. Sci. U.S.A. 102, 5727-5732
    • (2005) Proc. Natl. Acad. Sci. U.S.A , vol.102 , pp. 5727-5732
    • Zhao, H.1    Joseph, J.2    Fales, H.M.3    Sokoloski, E.A.4    Levine, R.L.5    Vasquez-Vivar, J.6    Kalyanaraman, B.7
  • 49
    • 38149142769 scopus 로고    scopus 로고
    • Detection of 2-hydroxyethidium in cellular systems: A unique marker product of superoxide and hydroethidine
    • Zielonka, J., Vasquez-Vivar, J. and Kalyanaraman, B. (2008) Detection of 2-hydroxyethidium in cellular systems: a unique marker product of superoxide and hydroethidine. Nat. Protoc. 3, 8-21
    • (2008) Nat. Protoc , vol.3 , pp. 8-21
    • Zielonka, J.1    Vasquez-Vivar, J.2    Kalyanaraman, B.3
  • 51
    • 0026492717 scopus 로고
    • Coelenterazine is a superoxide anion-sensitive chemiluminescent probe: Its usefulness in the assay of respiratory burst in neutrophils
    • Lucas, M. and Solano, F. (1992) Coelenterazine is a superoxide anion-sensitive chemiluminescent probe: its usefulness in the assay of respiratory burst in neutrophils. Anal. Biochem. 206, 273-277
    • (1992) Anal. Biochem , vol.206 , pp. 273-277
    • Lucas, M.1    Solano, F.2
  • 52
    • 0037458619 scopus 로고    scopus 로고
    • Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol
    • Han, D., Antunes, F., Canali, R., Rettori, D. and Cadenas, E. (2003) Voltage-dependent anion channels control the release of the superoxide anion from mitochondria to cytosol. J. Biol. Chem. 278, 5557-5563
    • (2003) J. Biol. Chem , vol.278 , pp. 5557-5563
    • Han, D.1    Antunes, F.2    Canali, R.3    Rettori, D.4    Cadenas, E.5
  • 53
    • 0036121191 scopus 로고    scopus 로고
    • Aconitase: Sensitive target and measure of superoxide
    • Gardner, P. R. (2002) Aconitase: sensitive target and measure of superoxide. Methods Enzmol. 349, 9-23
    • (2002) Methods Enzmol , vol.349 , pp. 9-23
    • Gardner, P.R.1
  • 54
    • 0021288856 scopus 로고
    • Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria
    • Boveris, A. (1984) Determination of the production of superoxide radicals and hydrogen peroxide in mitochondria. Methods Enzymol. 105, 429-435
    • (1984) Methods Enzymol , vol.105 , pp. 429-435
    • Boveris, A.1
  • 55
    • 0002622315 scopus 로고    scopus 로고
    • Kinetic measurement of mitochondrial oxygen radical production
    • CRC Press, Boca Raton
    • Barja, G. (1999) Kinetic measurement of mitochondrial oxygen radical production. In Methods in Aging Research, pp. 533-548, CRC Press, Boca Raton
    • (1999) Methods in Aging Research , pp. 533-548
    • Barja, G.1
  • 56
    • 0025943770 scopus 로고
    • Hydrogen peroxide production by mitochondria may be a biomarker of aging
    • Sohal, R. S. (1991) Hydrogen peroxide production by mitochondria may be a biomarker of aging. Mech. Ageing Dev. 60, 189-198
    • (1991) Mech. Ageing Dev , vol.60 , pp. 189-198
    • Sohal, R.S.1
  • 58
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: Biochemistry, pathophysiology and development of therapeutics
    • Szabo, C., Ischiropoulos, H. and Radi, R. (2007) Peroxynitrite: biochemistry, pathophysiology and development of therapeutics. Nat. Rev. 6, 662-680
    • (2007) Nat. Rev , vol.6 , pp. 662-680
    • Szabo, C.1    Ischiropoulos, H.2    Radi, R.3
  • 59
    • 0029857135 scopus 로고    scopus 로고
    • Mitochondrial superoxide production in the presence of nitric oxide leads to the formation of peroxynitrite
    • Packer, M. A., Porteous, C. M. and Murphy, M. P. (1996) Mitochondrial superoxide production in the presence of nitric oxide leads to the formation of peroxynitrite. Biochem. Mol. Biol. Int. 40, 527-534
    • (1996) Biochem. Mol. Biol. Int , vol.40 , pp. 527-534
    • Packer, M.A.1    Porteous, C.M.2    Murphy, M.P.3
  • 67
    • 0037438730 scopus 로고    scopus 로고
    • Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells
    • Imai, H. and Nakagawa, Y. (2003) Biological significance of phospholipid hydroperoxide glutathione peroxidase (PHGPx, GPx4) in mammalian cells. Free Radical Biol. Med. 34, 145-169
    • (2003) Free Radical Biol. Med , vol.34 , pp. 145-169
    • Imai, H.1    Nakagawa, Y.2
  • 68
    • 27244453860 scopus 로고    scopus 로고
    • The modulation of thiol redox state affects the production and metabolism of hydrogen peroxide by heart mitochondria
    • Rigobello, M. P., Folda, A., Scutari, G. and Bindoli, A. (2005) The modulation of thiol redox state affects the production and metabolism of hydrogen peroxide by heart mitochondria. Arch. Biochem. Biophys. 441, 112-122
    • (2005) Arch. Biochem. Biophys , vol.441 , pp. 112-122
    • Rigobello, M.P.1    Folda, A.2    Scutari, G.3    Bindoli, A.4
  • 69
    • 15044362438 scopus 로고    scopus 로고
    • Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins
    • Rhee, S. G., Kang, S. W., Jeong, W., Chang, T. S., Yang, K. S. and Woo, H. A. (2005) Intracellular messenger function of hydrogen peroxide and its regulation by peroxiredoxins. Curr. Opin. Cell Biol. 17, 183-189
    • (2005) Curr. Opin. Cell Biol , vol.17 , pp. 183-189
    • Rhee, S.G.1    Kang, S.W.2    Jeong, W.3    Chang, T.S.4    Yang, K.S.5    Woo, H.A.6
  • 70
    • 39949083765 scopus 로고    scopus 로고
    • Oxidation of mitochondrial peroxiredoxin 3 during the initiation of receptor-mediated apoptosis
    • Cox, A. G., Pullar, J. M., Hughes, G., Ledgerwood, E. C. and Hampton, M. B. (2008) Oxidation of mitochondrial peroxiredoxin 3 during the initiation of receptor-mediated apoptosis. Free Radical Biol. Med. 44, 1001-1009
    • (2008) Free Radical Biol. Med , vol.44 , pp. 1001-1009
    • Cox, A.G.1    Pullar, J.M.2    Hughes, G.3    Ledgerwood, E.C.4    Hampton, M.B.5
  • 71
    • 34547592709 scopus 로고    scopus 로고
    • Detection of reactive oxygen species-sensitive thiol proteins by redox difference gel electrophoresis: Implications for mitochondrial redox signaling
    • Hurd, T. R., Prime, T. A., Harbour, M. E., Lilley, K. S. and Murphy, M. P. (2007) Detection of reactive oxygen species-sensitive thiol proteins by redox difference gel electrophoresis: implications for mitochondrial redox signaling. J. Biol. Chem. 282, 22040-22051
    • (2007) J. Biol. Chem , vol.282 , pp. 22040-22051
    • Hurd, T.R.1    Prime, T.A.2    Harbour, M.E.3    Lilley, K.S.4    Murphy, M.P.5
  • 72
    • 0021891872 scopus 로고    scopus 로고
    • Holmgren, A. (1985) Thioredoxin. Annu. Rev. Biochem. 54, 237-271
    • Holmgren, A. (1985) Thioredoxin. Annu. Rev. Biochem. 54, 237-271
  • 74
    • 33745635338 scopus 로고    scopus 로고
    • Mitochondrial NADPH, transhydrogenase and disease
    • Rydström, J. (2006) Mitochondrial NADPH, transhydrogenase and disease. Biochim. Biophys. Acta 1757, 721-726
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 721-726
    • Rydström, J.1
  • 75
    • 0028339522 scopus 로고
    • Proton-translocating transhydrogenase and NAD- and NADP-linked isocitrate dehydrogenases operate in a substrate cycle which contributes to fine regulation of the tricarboxylic acid cycle activity in mitochondria
    • Sazanov, L. A. and Jackson, J. B. (1994) Proton-translocating transhydrogenase and NAD- and NADP-linked isocitrate dehydrogenases operate in a substrate cycle which contributes to fine regulation of the tricarboxylic acid cycle activity in mitochondria. FEBS Lett. 344, 109-116
    • (1994) FEBS Lett , vol.344 , pp. 109-116
    • Sazanov, L.A.1    Jackson, J.B.2
  • 78
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • Korshunov, S. S., Skulachev, V. P. and Starkov, A. A. (1997) High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 416, 15-18
    • (1997) FEBS Lett , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 79
    • 4043090717 scopus 로고    scopus 로고
    • Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane
    • Lambert, A. J. and Brand, M. D. (2004) Superoxide production by NADH:ubiquinone oxidoreductase (complex I) depends on the pH gradient across the mitochondrial inner membrane. Biochem. J. 382, 511-517
    • (2004) Biochem. J , vol.382 , pp. 511-517
    • Lambert, A.J.1    Brand, M.D.2
  • 81
    • 33847687662 scopus 로고    scopus 로고
    • Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain
    • Sazanov, L. A. (2007) Respiratory complex I: mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry 46, 2275-2288
    • (2007) Biochemistry , vol.46 , pp. 2275-2288
    • Sazanov, L.A.1
  • 82
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus
    • Sazanov, L. A. and Hinchliffe, P. (2006) Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311, 1430-1436
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchliffe, P.2
  • 83
    • 0014217470 scopus 로고
    • Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome β region of the respiratory chain of beef heart submitochondrial particles
    • Hinkle, P. C., Butow, R. A., Racker, E. and Chance, B. (1967) Partial resolution of the enzymes catalyzing oxidative phosphorylation. XV. Reverse electron transfer in the flavin-cytochrome β region of the respiratory chain of beef heart submitochondrial particles. J. Biol. Chem. 242, 5169-5173
    • (1967) J. Biol. Chem , vol.242 , pp. 5169-5173
    • Hinkle, P.C.1    Butow, R.A.2    Racker, E.3    Chance, B.4
  • 84
    • 0017406503 scopus 로고
    • Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria
    • Cadenas, E., Boveris, A., Ragan, C. I. and Stoppani, A. O. (1977) Production of superoxide radicals and hydrogen peroxide by NADH-ubiquinone reductase and ubiquinol-cytochrome c reductase from beef-heart mitochondria. Arch. Biochem. Biophys. 180, 248-257
    • (1977) Arch. Biochem. Biophys , vol.180 , pp. 248-257
    • Cadenas, E.1    Boveris, A.2    Ragan, C.I.3    Stoppani, A.O.4
  • 85
    • 53849099653 scopus 로고    scopus 로고
    • The production of reactive oxygen species by complex I
    • Hirst, J., King, M. S. and Pryde, K. R. (2008) The production of reactive oxygen species by complex I. Biochem. Soc. Trans. 36, 976-980
    • (2008) Biochem. Soc. Trans , vol.36 , pp. 976-980
    • Hirst, J.1    King, M.S.2    Pryde, K.R.3
  • 86
    • 0018393931 scopus 로고
    • NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation
    • Takeshige, K. and Minakami, S. (1979) NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation. Biochem. J. 180, 129-135
    • (1979) Biochem. J , vol.180 , pp. 129-135
    • Takeshige, K.1    Minakami, S.2
  • 87
    • 0034740585 scopus 로고    scopus 로고
    • m-Dependent and -independent production of reactive oxygen species by rat brain mitochondria
    • m-Dependent and -independent production of reactive oxygen species by rat brain mitochondria. J. Neurochem. 79, 266-277
    • (2001) J. Neurochem , vol.79 , pp. 266-277
    • Votyakova, T.V.1    Reynolds, I.J.2
  • 89
    • 0036319021 scopus 로고    scopus 로고
    • Generation of reactive oxygen species by the mitochondrial electron transport chain
    • Liu, Y., Fiskum, G. and Schubert, D. (2002) Generation of reactive oxygen species by the mitochondrial electron transport chain. J. Neurochem. 80, 780-787
    • (2002) J. Neurochem , vol.80 , pp. 780-787
    • Liu, Y.1    Fiskum, G.2    Schubert, D.3
  • 90
    • 0015363173 scopus 로고
    • The cellular production of hydrogen peroxide
    • Boveris, A., Oshino, N. and Chance, B. (1972) The cellular production of hydrogen peroxide. Biochem. J. 128, 617-630
    • (1972) Biochem. J , vol.128 , pp. 617-630
    • Boveris, A.1    Oshino, N.2    Chance, B.3
  • 91
    • 33750503465 scopus 로고    scopus 로고
    • The single subunit NADH dehydrogenase reduces generation of reactive oxygen species from complex I
    • Seo, B. B., Marella, M., Yagi, T. and Matsuno-Yagi, A. (2006) The single subunit NADH dehydrogenase reduces generation of reactive oxygen species from complex I. FEBS Lett. 580, 6105-6108
    • (2006) FEBS Lett , vol.580 , pp. 6105-6108
    • Seo, B.B.1    Marella, M.2    Yagi, T.3    Matsuno-Yagi, A.4
  • 92
    • 72949139589 scopus 로고
    • The interaction of energy and electron transfer reactions in mitochondria. I. General properties and nature of the products of succinate-linked reduction of pyridine nucleotide
    • Chance, B. and Hollunger, G. (1961) The interaction of energy and electron transfer reactions in mitochondria. I. General properties and nature of the products of succinate-linked reduction of pyridine nucleotide. J Biol. Chem. 236, 1534-1543
    • (1961) J Biol. Chem , vol.236 , pp. 1534-1543
    • Chance, B.1    Hollunger, G.2
  • 93
    • 0024297325 scopus 로고
    • Studies on the electron transfer pathway, topography of iron-sulfur centers, and site of coupling in NADH-Q oxidoreductase
    • Krishnamoorthy, G. and Hinkle, P. C. (1988) Studies on the electron transfer pathway, topography of iron-sulfur centers, and site of coupling in NADH-Q oxidoreductase. J. Biol. Chem. 263, 17566-17575
    • (1988) J. Biol. Chem , vol.263 , pp. 17566-17575
    • Krishnamoorthy, G.1    Hinkle, P.C.2
  • 94
    • 0024548927 scopus 로고
    • Generation of hydrogen peroxide by brain mitochondria: The effect of reoxygenation following postdecapitative ischemia
    • Cino, M. and Del Maestro, R. F. (1989) Generation of hydrogen peroxide by brain mitochondria: the effect of reoxygenation following postdecapitative ischemia. Arch. Biochem. Biophys. 269, 623-638
    • (1989) Arch. Biochem. Biophys , vol.269 , pp. 623-638
    • Cino, M.1    Del Maestro, R.F.2
  • 95
    • 4544354262 scopus 로고    scopus 로고
    • Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I)
    • Lambert, A. J. and Brand, M. D. (2004) Inhibitors of the quinone-binding site allow rapid superoxide production from mitochondrial NADH:ubiquinone oxidoreductase (complex I). J. Biol. Chem. 279, 39414-39420
    • (2004) J. Biol. Chem , vol.279 , pp. 39414-39420
    • Lambert, A.J.1    Brand, M.D.2
  • 96
    • 0030722043 scopus 로고    scopus 로고
    • Generating, partitioning, targeting and functioning of superoxide in mitochondria
    • Liu, S. S. (1997) Generating, partitioning, targeting and functioning of superoxide in mitochondria. Biosci. Rep. 17, 259-272
    • (1997) Biosci. Rep , vol.17 , pp. 259-272
    • Liu, S.S.1
  • 97
    • 43049141441 scopus 로고    scopus 로고
    • Diphenyleneiodonium acutely inhibits reactive oxygen species production by mitochondrial complex I during reverse, but not forward electron transport
    • Lambert, A. J., Buckingham, J. A., Boysen, H. M. and Brand, M. D. (2008) Diphenyleneiodonium acutely inhibits reactive oxygen species production by mitochondrial complex I during reverse, but not forward electron transport. Biochim. Biophys. Acta 1777, 397-403
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 397-403
    • Lambert, A.J.1    Buckingham, J.A.2    Boysen, H.M.3    Brand, M.D.4
  • 98
    • 43549110469 scopus 로고    scopus 로고
    • Dissociation of superoxide production by mitochondrial complex I from NAD(P)H redox state
    • Lambert, A. J., Buckingham, J. A. and Brand, M. D. (2008) Dissociation of superoxide production by mitochondrial complex I from NAD(P)H redox state. FEBS Lett. 582, 1711-1714
    • (2008) FEBS Lett , vol.582 , pp. 1711-1714
    • Lambert, A.J.1    Buckingham, J.A.2    Brand, M.D.3
  • 100
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens, J. F., Alexandre, A. and Lehninger, A. L. (1985) Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch. Biochem. Biophys. 237, 408-414
    • (1985) Arch. Biochem. Biophys , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 101
    • 0032545269 scopus 로고    scopus 로고
    • Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria
    • Zhang, L., Yu, L. and Yu, C. A. (1998) Generation of superoxide anion by succinate-cytochrome c reductase from bovine heart mitochondria. J. Biol. Chem. 273, 33972-33976
    • (1998) J. Biol. Chem , vol.273 , pp. 33972-33976
    • Zhang, L.1    Yu, L.2    Yu, C.A.3
  • 102
    • 0017818494 scopus 로고
    • The sites of superoxide anion generation in higher plant mitochondria
    • Rich, P. R. and Bonner, W. D. (1978) The sites of superoxide anion generation in higher plant mitochondria. Arch. Biochem. Biophys. 188, 206-213
    • (1978) Arch. Biochem. Biophys , vol.188 , pp. 206-213
    • Rich, P.R.1    Bonner, W.D.2
  • 103
    • 0018923857 scopus 로고
    • Tiron as a spin-trap for superoxide radicals produced by the respiratory chain of submitochondrial particles
    • Grigolava, I. V., Ksenzenko, M., Konstantinob, A. A., Tikhonov, A. N. and Kerimov, T. M. (1980) Tiron as a spin-trap for superoxide radicals produced by the respiratory chain of submitochondrial particles. Biochemisty (Moscow) 45, 75-82
    • (1980) Biochemisty (Moscow) , vol.45 , pp. 75-82
    • Grigolava, I.V.1    Ksenzenko, M.2    Konstantinob, A.A.3    Tikhonov, A.N.4    Kerimov, T.M.5
  • 104
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • Muller, F. L., Liu, Y. and Van Remmen, H. (2004) Complex III releases superoxide to both sides of the inner mitochondrial membrane. J. Biol. Chem. 279, 49064-49073
    • (2004) J. Biol. Chem , vol.279 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    Van Remmen, H.3
  • 105
    • 0030939089 scopus 로고    scopus 로고
    • On the virtual existence of superoxide anions in mitochondria: Thoughts regarding its role in pathophysiology
    • Forman, H. J. and Azzi, A. (1997) On the virtual existence of superoxide anions in mitochondria: thoughts regarding its role in pathophysiology. FASEB J. 11, 374-375
    • (1997) FASEB J , vol.11 , pp. 374-375
    • Forman, H.J.1    Azzi, A.2
  • 107
    • 4544226082 scopus 로고    scopus 로고
    • Generation of reactive oxygen species in the reaction catalyzed by α-ketoglutarate dehydrogenase
    • Tretter, L. and Adam-Vizi, V. (2004) Generation of reactive oxygen species in the reaction catalyzed by α-ketoglutarate dehydrogenase. J. Neurosci. 24, 7771-7778
    • (2004) J. Neurosci , vol.24 , pp. 7771-7778
    • Tretter, L.1    Adam-Vizi, V.2
  • 108
    • 0036408866 scopus 로고    scopus 로고
    • Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species
    • Bunik, V. I. and Sievers, C. (2002) Inactivation of the 2-oxo acid dehydrogenase complexes upon generation of intrinsic radical species. Eur. J. Biochem. 269, 5004-5015
    • (2002) Eur. J. Biochem , vol.269 , pp. 5004-5015
    • Bunik, V.I.1    Sievers, C.2
  • 109
    • 0036154857 scopus 로고    scopus 로고
    • Control of mitochondrial β-oxidation flux
    • Eaton, S. (2002) Control of mitochondrial β-oxidation flux. Prog. Lipid Res. 41, 197-239
    • (2002) Prog. Lipid Res , vol.41 , pp. 197-239
    • Eaton, S.1
  • 110
    • 0017293045 scopus 로고
    • Dihydroorotate-dependent superoxide production in rat brain and liver: A function of the primary dehydrogenase
    • Forman, H. J. and Kennedy, J. (1976) Dihydroorotate-dependent superoxide production in rat brain and liver: a function of the primary dehydrogenase. Arch. Biochem. Biophys. 173, 219-224
    • (1976) Arch. Biochem. Biophys , vol.173 , pp. 219-224
    • Forman, H.J.1    Kennedy, J.2
  • 111
    • 0030471636 scopus 로고    scopus 로고
    • Sequence and tissue-dependent RNA expression of mouse FAD-linked glycerol-3-phosphate dehydrogenase
    • Koza, R. A., Kozak, U. C., Brown, L. J., Leiter, E. H., MacDonald, M. J. and Kozak, L. P. (1996) Sequence and tissue-dependent RNA expression of mouse FAD-linked glycerol-3-phosphate dehydrogenase. Arch. Biochem. Biophys. 336, 97-104
    • (1996) Arch. Biochem. Biophys , vol.336 , pp. 97-104
    • Koza, R.A.1    Kozak, U.C.2    Brown, L.J.3    Leiter, E.H.4    MacDonald, M.J.5    Kozak, L.P.6
  • 112
    • 0036244950 scopus 로고    scopus 로고
    • Glycerophosphate-dependent hydrogen peroxide production by brown adipose tissue mitochondria and its activation by ferricyanide
    • Drahota, Z., Chowdhury, S. K., Floryk, D., Mracek, T., Wilhelm, J., Rauchova, H., Lenaz, G. and Houstek, J. (2002) Glycerophosphate-dependent hydrogen peroxide production by brown adipose tissue mitochondria and its activation by ferricyanide. J. Bioenerg. Biomembr. 34, 105-113
    • (2002) J. Bioenerg. Biomembr , vol.34 , pp. 105-113
    • Drahota, Z.1    Chowdhury, S.K.2    Floryk, D.3    Mracek, T.4    Wilhelm, J.5    Rauchova, H.6    Lenaz, G.7    Houstek, J.8
  • 114
    • 0141526414 scopus 로고    scopus 로고
    • Superoxide and hydrogen peroxide production by Drosophila mitochondria
    • Miwa, S., St-Pierre, J., Partridge, L. and Brand, M. D. (2003) Superoxide and hydrogen peroxide production by Drosophila mitochondria. Free Radical Biol. Med. 35, 938-948
    • (2003) Free Radical Biol. Med , vol.35 , pp. 938-948
    • Miwa, S.1    St-Pierre, J.2    Partridge, L.3    Brand, M.D.4
  • 115
    • 37849022071 scopus 로고    scopus 로고
    • Loss of the SdhB, but not the SdhA, subunit of complex II triggers reactive oxygen species-dependent hypoxia-inducible factor activation and tumorigenesis
    • Guzy, R. D., Sharma, B., Bell, E., Chandel, N. S. and Schumacker, P. T. (2008) Loss of the SdhB, but not the SdhA, subunit of complex II triggers reactive oxygen species-dependent hypoxia-inducible factor activation and tumorigenesis. Mol. Cell. Biol. 28, 718-731
    • (2008) Mol. Cell. Biol , vol.28 , pp. 718-731
    • Guzy, R.D.1    Sharma, B.2    Bell, E.3    Chandel, N.S.4    Schumacker, P.T.5
  • 116
    • 33646701679 scopus 로고    scopus 로고
    • Antioxidant protective mechanisms against reactive oxygen species (ROS) generated by mitochondrial P450 systems in steroidogenic cells
    • Hanukoglu, I. (2006) Antioxidant protective mechanisms against reactive oxygen species (ROS) generated by mitochondrial P450 systems in steroidogenic cells. Drug Metab. Rev. 38, 171-196
    • (2006) Drug Metab. Rev , vol.38 , pp. 171-196
    • Hanukoglu, I.1
  • 117
    • 0027328115 scopus 로고
    • Electron leakage from the mitochondrial NADPH-adrenodoxin reductase-adrenodoxin-P450scc (cholesterol side chain cleavage) system
    • Hanukoglu, I., Rapoport, R., Weiner, L. and Sklan, D. (1993) Electron leakage from the mitochondrial NADPH-adrenodoxin reductase-adrenodoxin-P450scc (cholesterol side chain cleavage) system. Arch. Biochem. Biophys. 305, 489-498
    • (1993) Arch. Biochem. Biophys , vol.305 , pp. 489-498
    • Hanukoglu, I.1    Rapoport, R.2    Weiner, L.3    Sklan, D.4
  • 119
    • 0042433242 scopus 로고    scopus 로고
    • 2 production by membrane potential and NAD(P)H redox state
    • 2 production by membrane potential and NAD(P)H redox state. J. Neurochem. 86, 1101-1107
    • (2003) J. Neurochem , vol.86 , pp. 1101-1107
    • Starkov, A.A.1    Fiskum, G.2
  • 121
    • 33747596652 scopus 로고    scopus 로고
    • Oxygen sensing by mitochondria at complex III: The paradox of increased reactive oxygen species during hypoxia
    • Guzy, R. D. and Schumacker, P. T. (2006) Oxygen sensing by mitochondria at complex III: the paradox of increased reactive oxygen species during hypoxia. Exp. Physiol. 91, 807-819
    • (2006) Exp. Physiol , vol.91 , pp. 807-819
    • Guzy, R.D.1    Schumacker, P.T.2
  • 123
    • 1342346637 scopus 로고    scopus 로고
    • 2-regulated gene expression: Transcriptional control of cardiorespiratory physiology by HIF-1
    • 2-regulated gene expression: transcriptional control of cardiorespiratory physiology by HIF-1. J. Appl. Physiol. 96, 1173-1177
    • (2004) J. Appl. Physiol , vol.96 , pp. 1173-1177
    • Semenza, G.L.1
  • 124
    • 18144378426 scopus 로고    scopus 로고
    • A targeted antioxidant reveals the importance of mitochondrial reactive oxygen species in the hypoxic signaling of HIF-1α
    • Sanjuan-Pla, A., Cervera, A. M., Apostolova, N., Garcia-Bou, R., Victor, V. M., Murphy, M. P. and McCreath, K. J. (2005) A targeted antioxidant reveals the importance of mitochondrial reactive oxygen species in the hypoxic signaling of HIF-1α. FEBS Lett. 579, 2669-2674
    • (2005) FEBS Lett , vol.579 , pp. 2669-2674
    • Sanjuan-Pla, A.1    Cervera, A.M.2    Apostolova, N.3    Garcia-Bou, R.4    Victor, V.M.5    Murphy, M.P.6    McCreath, K.J.7
  • 127
    • 2442664117 scopus 로고    scopus 로고
    • Endogenous NO regulates superoxide production at low oxygen concentrations by modifying the redox state of cytochrome c oxidase
    • Palacios-Callender, M., Quintero, M., Hollis, V. S., Springett, R. J. and Moncada, S. (2004) Endogenous NO regulates superoxide production at low oxygen concentrations by modifying the redox state of cytochrome c oxidase. Proc. Natl. Acad. Sci. U.S.A. 101, 7630-7635
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 7630-7635
    • Palacios-Callender, M.1    Quintero, M.2    Hollis, V.S.3    Springett, R.J.4    Moncada, S.5
  • 128
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman, K. B. and Ames, B. N. (1998) The free radical theory of aging matures. Physiol. Rev. 78, 547-581
    • (1998) Physiol. Rev , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 129
    • 0016430123 scopus 로고
    • The properties of hydrogen peroxide production under hyperoxic and hypoxic conditions of perfused rat liver
    • Oshino, N., Jamieson, D. and Chance, B. (1975) The properties of hydrogen peroxide production under hyperoxic and hypoxic conditions of perfused rat liver. Biochem. J. 146, 53-65
    • (1975) Biochem. J , vol.146 , pp. 53-65
    • Oshino, N.1    Jamieson, D.2    Chance, B.3
  • 130
    • 33847071146 scopus 로고    scopus 로고
    • Targeting antioxidants to mitochondria by conjugation to lipophilic cations
    • Murphy, M. P. and Smith, R. A. (2007) Targeting antioxidants to mitochondria by conjugation to lipophilic cations. Annu. Rev. Pharmacol. Toxicol. 47, 629-656
    • (2007) Annu. Rev. Pharmacol. Toxicol , vol.47 , pp. 629-656
    • Murphy, M.P.1    Smith, R.A.2
  • 131
    • 34547592709 scopus 로고    scopus 로고
    • Detection of reactive oxygen species-sensitive thiol proteins by redox difference gel electrophoresis: Implications for mitochondrial redox signaling
    • Hurd, T. R., Prime, T. A., Harbour, M. E., Lilley, K. S. and Murphy, M. P. (2007) Detection of reactive oxygen species-sensitive thiol proteins by redox difference gel electrophoresis: implications for mitochondrial redox signaling. J. Biol. Chem. 282, 22040-22051
    • (2007) J. Biol. Chem , vol.282 , pp. 22040-22051
    • Hurd, T.R.1    Prime, T.A.2    Harbour, M.E.3    Lilley, K.S.4    Murphy, M.P.5
  • 132
    • 33646678212 scopus 로고    scopus 로고
    • The three-dimensional structure of complex I from Yarrowia lipolytica: A highly dynamic enzyme
    • Radermacher, M., Ruiz, T., Clason, T., Benjamin, S., Brandt, U. and Zickermann, V. (2006) The three-dimensional structure of complex I from Yarrowia lipolytica: a highly dynamic enzyme. J. Struct. Biol. 154, 269-279
    • (2006) J. Struct. Biol , vol.154 , pp. 269-279
    • Radermacher, M.1    Ruiz, T.2    Clason, T.3    Benjamin, S.4    Brandt, U.5    Zickermann, V.6


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